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Fibrillar ß-lactoglobulin gels: Part 1. Fibril formation and structure

Research output: Contribution to journal › Article › peer-review

203 Citations (Scopus)

Abstract

As a prelude to experimental and theoretical work on the mechanical properties of fibrillar beta-lactoglobulin gels, this paper reports the structural characterization of beta-lactoglobulin fibrils by electron and atomic force microscopy (AFM), infrared and Raman spectroscopy, and powder X-ray diffraction. Aggregates formed by incubation of beta-lactoglobulin in various alcohol-water mixtures at pH 2, and in water-trifluoroethanol (TFE) at pH 7, were found to be wormlike (similar to7 nm in width and 1 mum in length), smoother, and seemingly stiffer fibrils formed on heating aqueous beta-lactoglobulin solutions at pH 2 and low ionic strength, although there was little evidence for the higher-order structures common in most amyloid-forming systems. Time-lapse AFM also revealed differences in the formation of these two fibril types: thermally induced aggregation occurring more cooperatively, in keeping with a nucleation and growth process. Only short stiff-rods (
Original languageEnglish
Pages (from-to)2408 - 2419
Number of pages12
JournalBIOMACROMOLECULES
Volume5
Issue number6
DOIs
Publication statusPublished - Nov 2004

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